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Hydrolytic Degradation of Polyethylene Terephthalate by Cutinase Enzyme Derived from Fungal Biomass–Molecular Characterization
Summary
Researchers isolated cutinase and lipase enzymes from Aspergillus tamarii and Penicillium crustosum fungi and demonstrated their ability to catalyze hydrolytic degradation of PET plastic, offering a potential biological route for plastic waste breakdown.
Polyethylene Terephthalate (PET) is utilized worldwide in plastic items, and its aggregation in the earth has turned into a worldwide concern. The hydrolysis of PET was done by cutinase and lipase enzyme. Lipase and cutinase enzymes were extracted from the fungal species isolated from soil. The isolated fungal species were identified as Aspergillus tamarii and Penicillium crustosum by 18S rRNA sequencing. Biodegradation test, cutinase enzyme-catalyzed PET hydrolysis, and different assays were conducted to elucidate PET hydrolysis by the extracted enzymes. These components incorporate cell surface connection inside biofilms, enzyme catalysts engaged with oxidation or hydrolysis of the plastic polymer, metabolic pathways in charge of take-up and osmosis of plastic parts, and synthetic factors favorable or inhibitory to the biodegradation procedure. The degradation of plastic was identified with terephthalic acid release (TPA) release as they are made of two monomeric units. Characterization studies such as FTIR and SEM analysis have exhibited loss of weight or change in physical properties, such as elasticity and the examination of Spectroscopic.
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